6r7b | pdb_00006r7b

Crystal structure of Csx1 in complex with cyclic oligoadenylate cOA4 conformation 1

spinqualitylabelsall models 6r7b, resolution 3.12Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6r7b is a 5 chain structure with sequence from Sulfolobus islandicus and Synthetic construct. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 3.12Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function F0NE21_SULIR Publication Abstract from PubMed Type III CRISPR-Cas multisubunit complexes cleave ssRNA and ssDNA. These activities promote the generation of cyclic oligoadenylate (cOA), which activates associated CRISPR-Cas RNases from the Csm/Csx families, triggering a massive RNA decay to provide immunity from genetic invaders. Here we present the structure of Sulfolobus islandicus (Sis) Csx1-cOA4 complex revealing the allosteric activation of its RNase activity. SisCsx1 is a hexamer built by a trimer of dimers. Each dimer forms a cOA4 binding site and a ssRNA catalytic pocket. cOA4 undergoes a conformational change upon binding in the second messenger binding site activating ssRNA degradation in the catalytic pockets. Activation is transmitted in an allosteric manner through an intermediate HTH domain, which joins the cOA4 and catalytic sites. The RNase functions in a sequential cooperative fashion, hydrolyzing phosphodiester bonds in 5'-C-C-3'. The degradation of cOA4 by Ring nucleases deactivates SisCsx1, suggesting that this enzyme could be employed in biotechnological applications. Structure of Csx1-cOA4 complex reveals the basis of RNA decay in Type III-B CRISPR-Cas.,Molina R, Stella S, Feng M, Sofos N, Jauniskis V, Pozdnyakova I, Lopez-Mendez B, She Q, Montoya G Nat Commun. 2019 Sep 20;10(1):4302. doi: 10.1038/s41467-019-12244-z. PMID:31541109 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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